ID CAIC_ECOBW Reviewed; 517 AA.
AC C4ZPW3;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 01-MAY-2013, entry version 31.
DE RecName: Full=Probable crotonobetaine/carnitine-CoA ligase;
DE EC=6.2.1.-;
GN Name=caiC; OrderedLocusNames=BWG_0035;
OS Escherichia coli (strain K12 / MC4100 / BW2952).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=595496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MC4100 / BW2952;
RX PubMed=19376874; DOI=10.1128/JB.00118-09;
RA Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L.,
RA Reeves P.R., Wang L.;
RT "Genomic sequencing reveals regulatory mutations and recombinational
RT events in the widely used MC4100 lineage of Escherichia coli K-12.";
RL J. Bacteriol. 191:4025-4029(2009).
CC -!- FUNCTION: Could catalyze the transfer of CoA to carnitine,
CC generating the initial carnitinyl-CoA needed for the CaiB reaction
CC cycle (By similarity).
CC -!- PATHWAY: Amine and polyamine metabolism; carnitine metabolism.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme
CC family.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACR64209.1; Type=Erroneous initiation;
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DR EMBL; CP001396; ACR64209.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_002925238.1; NC_012759.1.
DR ProteinModelPortal; C4ZPW3; -.
DR SMR; C4ZPW3; 9-517.
DR STRING; 595496.BWG_0035; -.
DR EnsemblBacteria; ACR64209; ACR64209; BWG_0035.
DR GeneID; 7953163; -.
DR KEGG; ebw:BWG_0035; -.
DR PATRIC; 18268946; VBIEscCol60876_0037.
DR eggNOG; COG0318; -.
DR HOGENOM; HOG000230001; -.
DR KO; K02182; -.
DR OMA; EESEWIL; -.
DR ProtClustDB; PRK08008; -.
DR BioCyc; ECOL595496:GI18-2668-MONOMER; -.
DR UniPathway; UPA00117; -.
DR GO; GO:0016878; F:acid-thiol ligase activity; IEA:InterPro.
DR GO; GO:0051108; F:carnitine-CoA ligase activity; IEA:InterPro.
DR GO; GO:0051109; F:crotonobetaine-CoA ligase activity; IEA:InterPro.
DR GO; GO:0009437; P:carnitine metabolic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_01524; CaiC; 1; -.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR023456; CaiC.
DR Pfam; PF00501; AMP-binding; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Complete proteome; Ligase.
FT CHAIN 1 517 Probable crotonobetaine/carnitine-CoA
FT ligase.
FT /FTId=PRO_0000383395.
SQ SEQUENCE 517 AA; 58559 MW; C7A307D16200D8E9 CRC64;
MDIIGGQHLR QMWDDLADVY GHKTALICES SGGVVNRYSY LELNQEINRT ANLFYTLGIR
KGDKVALHLD NCPEFIFCWF GLAKIGAIMV PINARLLCEE SAWILQNSQA CLLVTSAQFY
PMYQQIQQED ATQLRHICLT DVALPADDGV SSFTQLKNQQ PATLCYAPPL STDDTAEILF
TSGTTSRPKG VVITHYNLRF AGYYSAWQCA LRDDDVYLTV MPAFHIDCQC TAAMAAFSAG
ATFVLVEKYS ARAFWGQVQK YRATVTECIP MMIRTLMVQP PSANDQQHRL REVMFYLNLS
EQEKDAFCER FGVRLLTSYG MTETIVGIIG DRPGDKRRWP SIGRVGFCYE AEIRDDHNRP
LPAGEIGEIC IKGIPGKTIF KEYFLNPQAT AKVLEADGWL HTGDTGYRDE EDFFYFVDRR
CNMIKRGGEN VSCVELENII AAHPKIQDIV VVGIKDSIRD EAIKAFVVLN EGETLSEEEF
FRFCEQNMAK FKVPSYLEIR KDLPRNCSGK IIRKNLK
//